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Protein

Type-1 fimbrial protein, A chain

Gene

fimA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.

GO - Biological processi

  • cell adhesion Source: EcoCyc
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG10308-MONOMER.
ECOL316407:JW4277-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-1 fimbrial protein, A chain
Alternative name(s):
Type-1A pilin
Gene namesi
Name:fimA
Synonyms:pilA
Ordered Locus Names:b4314, JW4277
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10308. fimA.

Subcellular locationi

GO - Cellular componenti

  • pilus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Fimbrium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 182159Type-1 fimbrial protein, A chainPRO_0000009170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 84Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP04128.
PRIDEiP04128.

Interactioni

Protein-protein interaction databases

BioGridi4262746. 6 interactions.
DIPiDIP-9609N.
STRINGi511145.b4314.

Structurei

Secondary structure

1
182
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324Combined sources
Beta strandi45 – 517Combined sources
Beta strandi54 – 563Combined sources
Turni62 – 643Combined sources
Beta strandi67 – 715Combined sources
Beta strandi75 – 8410Combined sources
Helixi86 – 905Combined sources
Beta strandi93 – 975Combined sources
Beta strandi100 – 1023Combined sources
Helixi103 – 1053Combined sources
Turni115 – 1173Combined sources
Beta strandi120 – 1278Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi136 – 1383Combined sources
Helixi148 – 1503Combined sources
Beta strandi152 – 16716Combined sources
Beta strandi173 – 1808Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JTYNMR-A24-182[»]
2M5GNMR-A24-182[»]
2N7HNMR-A/B/C/D/E/F24-182[»]
3SQBX-ray3.20B/D/F/H37-182[»]
4DWHX-ray2.50B/D41-182[»]
ProteinModelPortaliP04128.
SMRiP04128. Positions 24-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04128.

Family & Domainsi

Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108RQP. Bacteria.
ENOG4111KX6. LUCA.
HOGENOMiHOG000260127.
InParanoidiP04128.
KOiK07345.
OMAiNDCDTSV.
OrthoDBiEOG63VC1D.
PhylomeDBiP04128.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
[Graphical view]
PfamiPF00419. Fimbrial. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIKTLAIVV LSALSLSSTA ALAAATTVNG GTVHFKGEVV NAACAVDAGS
60 70 80 90 100
VDQTVQLGQV RTASLAQEGA TSSAVGFNIQ LNDCDTNVAS KAAVAFLGTA
110 120 130 140 150
IDAGHTNVLA LQSSAAGSAT NVGVQILDRT GAALTLDGAT FSSETTLNNG
160 170 180
TNTIPFQARY FATGAATPGA ANADATFKVQ YQ
Length:182
Mass (Da):18,111
Last modified:February 1, 1995 - v2
Checksum:i35B2016BDD21A2C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201A → T in AAA24389 (PubMed:2858471).Curated
Sequence conflicti163 – 1631Missing in CAA25489 (PubMed:6147250).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00981 Genomic DNA. Translation: CAA25489.1.
M27603 Genomic DNA. Translation: AAA24389.1.
U14003 Genomic DNA. Translation: AAA97210.1.
U00096 Genomic DNA. Translation: AAC77270.1.
AP009048 Genomic DNA. Translation: BAE78307.1.
PIRiS56539. YQECT1.
RefSeqiNP_418734.1. NC_000913.3.
WP_000695564.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77270; AAC77270; b4314.
BAE78307; BAE78307; BAE78307.
GeneIDi948838.
KEGGiecj:JW4277.
eco:b4314.
PATRICi32124224. VBIEscCol129921_4455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00981 Genomic DNA. Translation: CAA25489.1.
M27603 Genomic DNA. Translation: AAA24389.1.
U14003 Genomic DNA. Translation: AAA97210.1.
U00096 Genomic DNA. Translation: AAC77270.1.
AP009048 Genomic DNA. Translation: BAE78307.1.
PIRiS56539. YQECT1.
RefSeqiNP_418734.1. NC_000913.3.
WP_000695564.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JTYNMR-A24-182[»]
2M5GNMR-A24-182[»]
2N7HNMR-A/B/C/D/E/F24-182[»]
3SQBX-ray3.20B/D/F/H37-182[»]
4DWHX-ray2.50B/D41-182[»]
ProteinModelPortaliP04128.
SMRiP04128. Positions 24-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262746. 6 interactions.
DIPiDIP-9609N.
STRINGi511145.b4314.

Proteomic databases

PaxDbiP04128.
PRIDEiP04128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77270; AAC77270; b4314.
BAE78307; BAE78307; BAE78307.
GeneIDi948838.
KEGGiecj:JW4277.
eco:b4314.
PATRICi32124224. VBIEscCol129921_4455.

Organism-specific databases

EchoBASEiEB0304.
EcoGeneiEG10308. fimA.

Phylogenomic databases

eggNOGiENOG4108RQP. Bacteria.
ENOG4111KX6. LUCA.
HOGENOMiHOG000260127.
InParanoidiP04128.
KOiK07345.
OMAiNDCDTSV.
OrthoDBiEOG63VC1D.
PhylomeDBiP04128.

Enzyme and pathway databases

BioCyciEcoCyc:EG10308-MONOMER.
ECOL316407:JW4277-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP04128.
PROiP04128.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
[Graphical view]
PfamiPF00419. Fimbrial. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of pilA, the gene encoding the structural component of type 1 pili in Escherichia coli."
    Orndorff P.E., Falkow S.
    J. Bacteriol. 162:454-457(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The fimA gene encoding the type-1 fimbrial subunit of Escherichia coli. Nucleotide sequence and primary structure of the protein."
    Klemm P.
    Eur. J. Biochem. 143:395-399(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiFIMA1_ECOLI
AccessioniPrimary (citable) accession number: P04128
Secondary accession number(s): Q2M5Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: February 1, 1995
Last modified: January 20, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.